NCPR1_ORYSJ
ID NCPR1_ORYSJ Reviewed; 695 AA.
AC Q7X7K8; A0A0P0WFQ6;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=NADPH--cytochrome P450 reductase 1 {ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000303|PubMed:23053415};
DE Short=CPR {ECO:0000255|HAMAP-Rule:MF_03212};
DE Short=OsCPR1 {ECO:0000303|PubMed:23053415};
DE Short=P450R {ECO:0000255|HAMAP-Rule:MF_03212};
DE EC=1.6.2.4 {ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:23053415};
GN Name=CPR1 {ECO:0000303|PubMed:23053415};
GN OrderedLocusNames=Os04g0653400 {ECO:0000312|EMBL:BAS91389.1};
GN ORFNames=OSJNBa0060D06.20 {ECO:0000312|EMBL:CAE03554.2},
GN OSJNBb0022F16.2 {ECO:0000312|EMBL:CAE01547.2};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RG The rice full-length cDNA consortium;
RT "Oryza sativa full length cDNA.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INDUCTION BY JASMONATE.
RX PubMed=11332734; DOI=10.1094/mpmi.2001.14.5.685;
RA Xiong L., Lee M.W., Qi M., Yang Y.;
RT "Identification of defense-related rice genes by suppression subtractive
RT hybridization and differential screening.";
RL Mol. Plant Microbe Interact. 14:685-692(2001).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND INDUCTION.
RX PubMed=23053415; DOI=10.1007/s00449-012-0787-0;
RA Park S., Kim Y.S., Rupasinghe S.G., Schuler M.A., Back K.;
RT "Rice P450 reductases differentially affect P450-mediated metabolism in
RT bacterial expression systems.";
RL Bioprocess Biosyst. Eng. 36:325-331(2013).
CC -!- FUNCTION: This enzyme is required for electron transfer from NADP to
CC cytochrome P450 in microsomes (By similarity) (PubMed:23053415). It can
CC also provide electron transfer to heme oxygenase and cytochrome B5 (By
CC similarity). Can reduce cytochrome c in vitro (PubMed:23053415).
CC {ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:23053415}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2
CC reduced [cytochrome P450]; Xref=Rhea:RHEA:24040, Rhea:RHEA-
CC COMP:14627, Rhea:RHEA-COMP:14628, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:55376, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:60344; EC=1.6.2.4; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03212, ECO:0000269|PubMed:23053415};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24041;
CC Evidence={ECO:0000269|PubMed:23053415};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03212};
CC Note=Binds 1 FAD per monomer. {ECO:0000255|HAMAP-Rule:MF_03212};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03212};
CC Note=Binds 1 FMN per monomer. {ECO:0000255|HAMAP-Rule:MF_03212};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.0 uM for cytochrome c {ECO:0000269|PubMed:23053415};
CC Vmax=15.07 umol/min/mg enzyme with cytochrome c as substrate
CC {ECO:0000269|PubMed:23053415};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:23053415}; Single-
CC pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03212}; Cytoplasmic
CC side {ECO:0000255|HAMAP-Rule:MF_03212}.
CC -!- INDUCTION: Induced by drought stress, acifluorfen and cadmium
CC (PubMed:23053415). Induced by jasmonate (JA) (PubMed:11332734).
CC {ECO:0000269|PubMed:11332734, ECO:0000269|PubMed:23053415}.
CC -!- SIMILARITY: Belongs to the NADPH--cytochrome P450 reductase family.
CC {ECO:0000255|HAMAP-Rule:MF_03212}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
CC pyridine nucleotide cytochrome reductase family. {ECO:0000255|HAMAP-
CC Rule:MF_03212}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the flavodoxin
CC family. {ECO:0000255|HAMAP-Rule:MF_03212}.
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DR EMBL; AL606446; CAE01547.2; -; Genomic_DNA.
DR EMBL; AL606690; CAE03554.2; -; Genomic_DNA.
DR EMBL; AP014960; BAS91389.1; -; Genomic_DNA.
DR EMBL; AK243608; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015636692.1; XM_015781206.1.
DR AlphaFoldDB; Q7X7K8; -.
DR SMR; Q7X7K8; -.
DR STRING; 4530.OS04T0653400-01; -.
DR PaxDb; Q7X7K8; -.
DR PRIDE; Q7X7K8; -.
DR EnsemblPlants; Os04t0653400-01; Os04t0653400-01; Os04g0653400.
DR GeneID; 4337244; -.
DR Gramene; Os04t0653400-01; Os04t0653400-01; Os04g0653400.
DR KEGG; osa:4337244; -.
DR eggNOG; KOG1158; Eukaryota.
DR HOGENOM; CLU_001570_17_3_1; -.
DR InParanoid; Q7X7K8; -.
DR OMA; NTNYLWA; -.
DR OrthoDB; 318396at2759; -.
DR SABIO-RK; Q7X7K8; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0010181; F:FMN binding; IBA:GO_Central.
DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR Gene3D; 1.20.990.10; -; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR HAMAP; MF_03212; NCPR; 1.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001094; Flavdoxin-like.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR023208; P450R.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PIRSF; PIRSF000208; P450R; 1.
DR PRINTS; PR00369; FLAVODOXIN.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52218; SSF52218; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; FAD; Flavoprotein; FMN; Membrane; NADP;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..695
FT /note="NADPH--cytochrome P450 reductase 1"
FT /id="PRO_0000451428"
FT TOPO_DOM 1..29
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT TOPO_DOM 51..695
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT DOMAIN 85..235
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT DOMAIN 291..540
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 91..96
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 146..149
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 184..193
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 219
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 311
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 473..476
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 491..493
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 507..510
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 554
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 615..616
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 621..625
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 657
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 695
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
SQ SEQUENCE 695 AA; 76172 MW; 56A8C2C0A02E26B6 CRC64;
MALALEAARS WAASVLPPEL AAAAGGDPLA ALAATAAALV AGVVILAVWF RSGGGAPPKA
AAPPPRPPPV KIEADADADD GRKRVTVFFG TQTGTAEGFA KAMAEEARAR YEKAVFKVVD
LDDYAAEDEE YEEKLRKETI VLLFLATYGD GEPTDNAARF YKWFTEGKEK EVWLKDLKYA
VFGLGNRQYE HFNKVAKVVD ELLEEQGGKR LVPVGLGDDD QCIEDDFTAW KEQVWPELDQ
LLRDEDDTTG ASTPYTAAIP EYRIVFIDKS DVSFQDKSWS LANGSGVIDI HHPVRSNVAV
RKELHKPASD RSCIHLEFDI SGTGLVYETG DHVGVYSENA IETVEQAEKL LDLSPDTFFS
VHADAEDGSP RKGGGSLAPP FPSPCTLRTA LLRYADLLNS PKKAALVALA AHASDLAEAE
RLRFLASPAG KDEYSQWVVA SQRSLLEVMA AFPSAKPPLG VFFAAVAPRL QPRYYSISSS
PKMAPSRIHV TCALVYGPTP TGRIHQGVCS TWMKNAIPSE YSEECSWAPI YVRQSNFKLP
ADPTTPIIMI GPGTGLAPFR GFLQERLALK QSGVELGNSV LFFGCRNRNM DYIYEDELQN
FIQEGALSEL IVAFSREGPA KEYVQHKMTE KATEIWNIVS QGGYIYVCGD AKGMARDVHR
ALHTIVQEQG SLDSSKTESY VKSLQMDGRY LRDVW
